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O14526

- FCHO1_HUMAN

UniProt

O14526 - FCHO1_HUMAN

Protein

FCH domain only protein 1

Gene

FCHO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    Functions in an early step of clathrin-mediated endocytosis. Has both a membrane binding/bending activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. May regulate Bmp signaling by regulating clathrin-mediated endocytosis of Bmp receptors.1 Publication

    GO - Molecular functioni

    1. AP-2 adaptor complex binding Source: MGI
    2. protein binding Source: IntAct

    GO - Biological processi

    1. clathrin coat assembly Source: UniProtKB
    2. clathrin-mediated endocytosis Source: UniProtKB

    Keywords - Biological processi

    Endocytosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FCH domain only protein 1
    Gene namesi
    Name:FCHO1
    Synonyms:KIAA0290
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:29002. FCHO1.

    Subcellular locationi

    Membraneclathrin-coated pit 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side 2 Publications
    Note: Associated with forming but not mature clathrin-coated vesicles. The recruitment to coated-pits precede the one of clathrin and the adaptor protein complex AP-2. According to PubMed:17617719 it may also dynamically associate with Golgi/TGN membranes.

    GO - Cellular componenti

    1. coated pit Source: UniProtKB
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Coated pit, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134870625.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 889889FCH domain only protein 1PRO_0000271759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei616 – 6161Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO14526.
    PaxDbiO14526.
    PRIDEiO14526.

    PTM databases

    PhosphoSiteiO14526.

    Expressioni

    Gene expression databases

    ArrayExpressiO14526.
    BgeeiO14526.
    CleanExiHS_FCHO1.
    GenevestigatoriO14526.

    Organism-specific databases

    HPAiHPA041653.

    Interactioni

    Subunit structurei

    May oligomerize and form homotetramer By similarity. Interacts with AP2A2 and AP2B1; 2 subunits of the adaptor protein complex AP-2. Interacts with DAB2. Interacts with clathrin (CLTC or CLTCL1). Interacts with EPS15, EPS15R and ITSN1. Interacts with AGFG1 and CALM. May interact with ACVR1; linking this receptor to clathrin-mediated endocytosis.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    A7BFV92EBI-719823,EBI-6095043From a different organism.

    Protein-protein interaction databases

    BioGridi116764. 5 interactions.
    IntActiO14526. 4 interactions.
    MINTiMINT-7979234.
    STRINGi9606.ENSP00000252771.

    Structurei

    3D structure databases

    ProteinModelPortaliO14526.
    SMRiO14526. Positions 1-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8382FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini625 – 888264MHDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 275275Mediates membrane-bindingAdd
    BLAST
    Regioni267 – 442176Mediates interaction with the adaptor protein complex AP-2Add
    BLAST
    Regioni609 – 889281Mediates interaction with AGFG1, CALM, DAB2, EPS15, EPS15R, ITSN1 and clathrinAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili156 – 19540Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi375 – 3784Poly-Ala
    Compositional biasi465 – 4684Poly-Ser
    Compositional biasi480 – 56182Pro-richAdd
    BLAST
    Compositional biasi671 – 6744Poly-Pro

    Sequence similaritiesi

    Belongs to the FCHO family.Curated
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG324072.
    HOGENOMiHOG000231544.
    HOVERGENiHBG081524.
    InParanoidiO14526.
    OrthoDBiEOG712TVK.
    PhylomeDBiO14526.
    TreeFamiTF328986.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR028565. MHD.
    IPR018808. Muniscin_C.
    [Graphical view]
    PfamiPF00611. FCH. 1 hit.
    PF10291. muHD. 1 hit.
    [Graphical view]
    SMARTiSM00055. FCH. 1 hit.
    [Graphical view]
    PROSITEiPS50133. FCH. 1 hit.
    PS51072. MHD. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14526-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSYFGEHFWG EKNHGFEVLY HSVKQGPIST KELADFIRER ATIEETYSKA    50
    MAKLSKLASN GTPMGTFAPL WEVFRVSSDK LALCHLELTR KLQDLIKDVL 100
    RYGEEQLKTH KKCKEEVVST LDAVQVLSGV SQLLPKSREN YLNRCMDQER 150
    LRRESTSQKE MDKAETKTKK AAESLRRSVE KYNSARADFE QKMLDSALRF 200
    QAMEETHLRH MKALLGSYAH SVEDTHVQIG QVHEEFKQNI ENVSVEMLLR 250
    KFAESKGTGR EKPGPLDFEA YSAAALQEAM KRLRGAKAFR LPGLSRRERE 300
    PEPPAAVDFL EPDSGTCPEV DEEGFTVRPD VTQNSTAEPS RFSSSDSDFD 350
    DEEPRKFYVH IKPAPARAPA CSPEAAAAQL RATAGSLILP PGPGGTMKRH 400
    SSRDAAGKPQ RPRSAPRTSS CAERLQSEEQ VSKNLFGPPL ESAFDHEDFT 450
    GSSSLGFTSS PSPFSSSSPE NVEDSGLDSP SHAAPGPSPD SWVPRPGTPQ 500
    SPPSCRAPPP EARGIRAPPL PDSPQPLASS PGPWGLEALA GGDLMPAPAD 550
    PTAREGLAAP PRRLRSRKVS CPLTRSNGDL SRSLSPSPLG SSAASTALER 600
    PSFLSQTGHG VSRGPSPVVL GSQDALPIAT AFTEYVHAYF RGHSPSCLAR 650
    VTGELTMTFP AGIVRVFSGT PPPPVLSFRL VHTTAIEHFQ PNADLLFSDP 700
    SQSDPETKDF WLNMAALTEA LQRQAEQNPT ASYYNVVLLR YQFSRPGPQS 750
    VPLQLSAHWQ CGATLTQVSV EYGYRPGATA VPTPLTNVQI LLPVGEPVTN 800
    VRLQPAATWN LEEKRLTWRL PDVSEAGGSG RLSASWEPLS GPSTPSPVAA 850
    QFTSEGTTLS GVDLELVGSG YRMSLVKRRF ATGMYLVSC 889
    Length:889
    Mass (Da):96,861
    Last modified:January 9, 2007 - v2
    Checksum:i8CDA1F24F42256D2
    GO
    Isoform 2 (identifier: O14526-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         883-889: GMYLVSC → AAPPQG

    Note: No experimental confirmation available.

    Show »
    Length:888
    Mass (Da):96,629
    Checksum:i27DB24B8191372A9
    GO
    Isoform 3 (identifier: O14526-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-50: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:839
    Mass (Da):91,013
    Checksum:i4CC94A2046D108CE
    GO

    Sequence cautioni

    The sequence BAA22959.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5050Missing in isoform 3. 1 PublicationVSP_046906Add
    BLAST
    Alternative sequencei883 – 8897GMYLVSC → AAPPQG in isoform 2. 1 PublicationVSP_022338

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006628 mRNA. Translation: BAA22959.1. Different initiation.
    AK291410 mRNA. Translation: BAF84099.1.
    AK303623 mRNA. Translation: BAG64632.1.
    AC008761 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84629.1.
    BC028021 mRNA. Translation: AAH28021.1.
    BC041130 mRNA. Translation: AAH41130.1.
    CCDSiCCDS32955.1. [O14526-1]
    CCDS59366.1. [O14526-3]
    PIRiT00039.
    RefSeqiNP_001154829.1. NM_001161357.1.
    NP_001154830.1. NM_001161358.1. [O14526-1]
    NP_001154831.1. NM_001161359.1. [O14526-3]
    NP_055937.1. NM_015122.2. [O14526-1]
    XP_006722764.1. XM_006722701.1. [O14526-1]
    XP_006722765.1. XM_006722702.1. [O14526-1]
    UniGeneiHs.96485.

    Genome annotation databases

    EnsembliENST00000252771; ENSP00000252771; ENSG00000130475. [O14526-1]
    ENST00000594202; ENSP00000473001; ENSG00000130475.
    ENST00000595033; ENSP00000472668; ENSG00000130475. [O14526-3]
    ENST00000596536; ENSP00000470731; ENSG00000130475. [O14526-1]
    ENST00000596951; ENSP00000472417; ENSG00000130475. [O14526-1]
    ENST00000600676; ENSP00000470493; ENSG00000130475. [O14526-1]
    GeneIDi23149.
    KEGGihsa:23149.
    UCSCiuc002nhg.3. human. [O14526-2]
    uc002nhh.2. human. [O14526-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006628 mRNA. Translation: BAA22959.1 . Different initiation.
    AK291410 mRNA. Translation: BAF84099.1 .
    AK303623 mRNA. Translation: BAG64632.1 .
    AC008761 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84629.1 .
    BC028021 mRNA. Translation: AAH28021.1 .
    BC041130 mRNA. Translation: AAH41130.1 .
    CCDSi CCDS32955.1. [O14526-1 ]
    CCDS59366.1. [O14526-3 ]
    PIRi T00039.
    RefSeqi NP_001154829.1. NM_001161357.1.
    NP_001154830.1. NM_001161358.1. [O14526-1 ]
    NP_001154831.1. NM_001161359.1. [O14526-3 ]
    NP_055937.1. NM_015122.2. [O14526-1 ]
    XP_006722764.1. XM_006722701.1. [O14526-1 ]
    XP_006722765.1. XM_006722702.1. [O14526-1 ]
    UniGenei Hs.96485.

    3D structure databases

    ProteinModelPortali O14526.
    SMRi O14526. Positions 1-269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116764. 5 interactions.
    IntActi O14526. 4 interactions.
    MINTi MINT-7979234.
    STRINGi 9606.ENSP00000252771.

    PTM databases

    PhosphoSitei O14526.

    Proteomic databases

    MaxQBi O14526.
    PaxDbi O14526.
    PRIDEi O14526.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252771 ; ENSP00000252771 ; ENSG00000130475 . [O14526-1 ]
    ENST00000594202 ; ENSP00000473001 ; ENSG00000130475 .
    ENST00000595033 ; ENSP00000472668 ; ENSG00000130475 . [O14526-3 ]
    ENST00000596536 ; ENSP00000470731 ; ENSG00000130475 . [O14526-1 ]
    ENST00000596951 ; ENSP00000472417 ; ENSG00000130475 . [O14526-1 ]
    ENST00000600676 ; ENSP00000470493 ; ENSG00000130475 . [O14526-1 ]
    GeneIDi 23149.
    KEGGi hsa:23149.
    UCSCi uc002nhg.3. human. [O14526-2 ]
    uc002nhh.2. human. [O14526-1 ]

    Organism-specific databases

    CTDi 23149.
    GeneCardsi GC19P017862.
    HGNCi HGNC:29002. FCHO1.
    HPAi HPA041653.
    MIMi 613437. gene.
    neXtProti NX_O14526.
    PharmGKBi PA134870625.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324072.
    HOGENOMi HOG000231544.
    HOVERGENi HBG081524.
    InParanoidi O14526.
    OrthoDBi EOG712TVK.
    PhylomeDBi O14526.
    TreeFami TF328986.

    Miscellaneous databases

    ChiTaRSi FCHO1. human.
    GenomeRNAii 23149.
    NextBioi 44466.
    PROi O14526.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14526.
    Bgeei O14526.
    CleanExi HS_FCHO1.
    Genevestigatori O14526.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR028565. MHD.
    IPR018808. Muniscin_C.
    [Graphical view ]
    Pfami PF00611. FCH. 1 hit.
    PF10291. muHD. 1 hit.
    [Graphical view ]
    SMARTi SM00055. FCH. 1 hit.
    [Graphical view ]
    PROSITEi PS50133. FCH. 1 hit.
    PS51072. MHD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins."
      Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
      DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Brain and Thymus.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Blood.
    6. "Dynamic behavior of FCHO1 revealed by live-cell imaging microscopy: its possible involvement in clathrin-coated vesicle formation."
      Sakaushi S., Inoue K., Zushi H., Senda-Murata K., Fukada T., Oka S., Sugimoto K.
      Biosci. Biotechnol. Biochem. 71:1764-1768(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "FCHo proteins are nucleators of clathrin-mediated endocytosis."
      Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T.
      Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CLATHRIN-COATED PITS NUCLEATION, SUBCELLULAR LOCATION.
    9. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
      Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
      Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIPID-BINDING, INTERACTION WITH ACVR1; AGFG1; AP2A2; AP2B1; CALM; DAB2; EPS15; EPS15R; ITSN1 AND CLATHRIN.

    Entry informationi

    Entry nameiFCHO1_HUMAN
    AccessioniPrimary (citable) accession number: O14526
    Secondary accession number(s): A6NHE6
    , A8K5U5, B4E120, Q05C93, Q8IW22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3